Translation elongation is a complicated process where amino acids are added to the peptide chain within the ribosomes for protein production. In each elongation cycle the ribosome samples different aminoacyl tRNA (aa-tRNA) species to find a match for the mRNA codon. There are around 40-45 different tRNA species in E. coli and on an average all of them have to be sampled to find a match. Then the aa-tRNA transfers the amino acid to the growing peptide chain and the deacylated tRNA leaves. For cells growing in good growth medium, the entire cycle takes around 50 ms. Different proteins (elongation factors) are involved in different steps of the elongations cycle, the two major ones being EF-Tu and EF-G. EF-Tu forms a ternary complex with aa-tRNA and GTP and thus brings the aa-tRNA to the ribosome. The elongation cycle has been studied in great detail using both bulk and single molecule experiments, but the initial interaction of ternary complex with ribosome (specifically with L7/L12 stalk) is not properly understood, mainly due to the lack of structural data. Using superresolution imaging (PALM), we have studied dynamics of ternary complex and L7/L12 stalk interaction. Our results have shown that the interaction is highly transient and multiple ternary complexes can bind to translating ribosomes at the same time. This high binding stoichiometry can lead to high concentration of tRNA around ribosomes for efficient translation. We have further incorporated the effects of nutrient limitation, osmotic effects and various translation halting drug treatment on the dynamics of EF-Tu/ternary complex